ANA ISABEL
AZUAGA FORTES
PROFESORA TITULAR DE UNIVERSIDAD
FRANCISCO
CONEJERO LARA
CATEDRÁTICO DE UNIVERSIDAD
Publicaciones en las que colabora con FRANCISCO CONEJERO LARA (12)
2014
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Correction: Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: An experimental kinetics study (PLoS ONE)
PLoS ONE
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Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis
Physical Chemistry Chemical Physics, Vol. 16, Núm. 7, pp. 2989-3000
2012
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Aplicación de las TICS a las enseñanzas prácticas de química física en el contexto del EEES (09-144)
Innovación docente y buenas prácticas en la Universidad de Granada. (Editorial Universidad de Granada), pp. 155-162
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Characterization of Oligomers of Heterogeneous Size as Precursors of Amyloid Fibril Nucleation of an SH3 Domain: An Experimental Kinetics Study
PLoS ONE, Vol. 7, Núm. 11
2010
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Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology
Biophysical Journal, Vol. 99, Núm. 11, pp. 3801-3810
2009
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A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state
FEBS Letters, Vol. 583, Núm. 4, pp. 801-806
2002
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Unfolding and aggregation during the thermal denaturation of streptokinase
European Journal of Biochemistry, Vol. 269, Núm. 16, pp. 4121-4133
1999
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Expression and characterization of the intact N-terminal domain of streptokinase
Protein Science, Vol. 8, Núm. 2, pp. 443-446
1998
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Analysis of the interactions between streptokinase domains and human plasminogen
Protein Science, Vol. 7, Núm. 10, pp. 2190-2199
1997
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Differential scanning calorimetry of thermolysin and its 255-316 and 205-316 C-terminal fragments
Reactive and Functional Polymers, Vol. 34, Núm. 1, pp. 113-120
1996
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Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance
Protein Science, Vol. 5, Núm. 12, pp. 2583-2591
1995
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The thermodynamics of association and unfolding of the 205-316 C-terminal fragment of thermolysin
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1252, Núm. 1, pp. 95-102